Research workbench

HIV-1 RT/9-cl tibo

Analyse HIV-1 RT/9-cl tibo in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1TVR
Type: protein
Length: 985 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Reverse transcriptase
EC: 2.7.7.49
UniProt: P03366
Ligands: TB9
Pockets: 15 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 31% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Reverse transcriptase (EC 2.7.7.49)	protein	558	30% helix, 16% strand	P03366
B	Reverse transcriptase (EC 2.7.7.49)	protein	427	33% helix, 13% strand	P03366

Ligands and binding sites

TB9 · 4-chloro-8-methyl-7-(3-methyl-but-2-enyl)-6,7,8,9-tetrahydro-2H-2,7,9A-triaza-benzo[cd]azulene-1-thione · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	988	0.82	0.83	83	empty
2	768	0.79	0.82	78	TB9
3	797	0.74	0.79	71	empty
4	321	0.68	0.82	38	empty
5	157	0.65	0.86	29	empty

Interfaces

1 interface between chains.

A–B · 2519 Å² buried · 24 hydrogen bonds · protein-protein

Compared structures

1TVR · HIV-1 RT/9-cl tibo · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P03366
Elsewhere: RCSB PDB 1TVR · PDBe 1TVR · UniProt P03366

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